Structural and Functional Analysis of Transmembrane Segment IV of the Salt Tolerance Protein Sod2*

Ullah, A.K.M. Shahid; Kemp, Grant; Lee, Brian; Alves, Claudia; Young, Howard S.; Sykes, Brian D.; Fliegel, Larry

doi:10.1074/jbc.m113.483065

Cited by 10 publications

(26 citation statements)

References 65 publications

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“…Several of these amino acid residues seem to be conserved in the Na + /H + antiporters of all organisms and are proposed to be directly involved in the translocation of ions and protons through the antiporter. For S. pombe Sod2/NHE1, alanine scanning approaches or construction of cysteine‐free mutants recently revealed new residues important for antiporter activity and structure (Ullah et al, ; Ullah, El‐Magd, & Fliegel, ) and have led to the proposal of a model with 13 transmembrane segments and an outward‐oriented N‐terminus (Dutta & Fliegel, ). Another approach, identifying the amino acids important for the substrate specificity of yeast antiporters, revealed a group of four amino acid residues located in three different transmembrane segments, which together form a hydrophobic filter whose size determines the substrate specificity.…”

Section: The Nha Efflux Systemmentioning

confidence: 99%

Monovalent cation transporters at the plasma membrane in yeasts

Ariño

Ramos

Sychrová

2018

Yeast

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Maintenance of proper intracellular concentrations of monovalent cations, mainly sodium and potassium, is a requirement for survival of any cell. In the budding yeast Saccharomyces cerevisiae, monovalent cation homeostasis is determined by the active extrusion of protons through the Pma1 H -ATPase (reviewed in another chapter of this issue), the influx and efflux of these cations through the plasma membrane transporters (reviewed in this chapter), and the sequestration of toxic cations into the vacuoles. Here, we will describe the structure, function, and regulation of the plasma membrane transporters Trk1, Trk2, Tok1, Nha1, and Ena1, which play a key role in maintaining physiological intracellular concentrations of Na , K , and H , both under normal growth conditions and in response to stress.

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Section: The Nha Efflux Systemmentioning

confidence: 99%

Monovalent cation transporters at the plasma membrane in yeasts

Ariño

Ramos

Sychrová

2018

Yeast

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“…We recently demonstrated that there are many critical residues present within amino acids 360–378 and a similarity to TM 11 of Ec NhaA. Earlier , we also examined a putative TM segment of Sp NHE1 from amino acids 126 to 152. It also had similarity to TM 4 of NhaA and TM 4 of h NHE1 (see below).…”

Section: Protein Structurementioning

confidence: 99%

“…Return of this gene restores salt tolerance. This allows the indirect assay of Sp NHE1 by assay of S. pombe growth in salt containing media . Other plasma membrane NHEs such as S. cerevisiae Nha1p ( Sc Nha1p) and Z. rouxii Sod2 ( Zr Sod2p) have also been characterized to varying degrees .…”

Section: Introductionmentioning

confidence: 99%

“…The structure of mammalian Na + /H + exchangers has not been deduced, although nuclear magnetic resonance (NMR) structures of isolated transmembrane (TM) segments of human Na + /H + exchanger isoform 1 ( h NHE1) have been reported . Structural information of two critical TM segments of Sp NHE1 has also been reported . However, despite the presence of this structural data, few correlations have been made between this data and mutational effects in Na + /H + antiporters of yeast species.…”

Section: Introductionmentioning

confidence: 99%

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Structure and function of yeast and fungal Na⁺/H⁺ antiporters

Dutta

Fliegel

2017

IUBMB Life

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Sodium proton antiporters (or sodium proton exchangers [NHEs]) are a critical family of membrane proteins that exchange sodium for protons across cell membranes. In yeast and plants, their primary function is to keep the sodium concentration low inside the cytoplasm. One class of NHE constitutively expressed in yeast is the plasma membrane Na 1 /H 1 antiporter, and another class is expressed on the endosomal/ vacuolar membrane. At present, four bacterial plasma membrane antiporter structures are known and nuclear magnetic resonance structures are available for the membrane spanning transmembrane helices of mammalian and yeast NHEs.Additionally, a vast amount of mutational data are available on the role of individual amino acids and critical motifs involved in transport. We combine this information to obtain a more detailed picture of the yeast NHE plasma membrane protein and review mechanisms of transport, conserved motifs, unique residues important in function, and regulation of these proteins. The Na

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“…2E). A similar discontinuity is present in the equivalent helix of SpNHE1 (Ullah et al 2013). A peptide of TM6-7 was examined earlier by NMR.…”

Section: Tm6 and Tm7mentioning

confidence: 58%

Molecular modeling and inhibitor docking analysis of the Na⁺/H⁺exchanger isoform one

Dutta

Fliegel

2019

Biochem. Cell Biol.

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Na/H exchanger isoform one (NHE1) is a mammalian plasma membrane protein that removes intracellular protons, thereby elevating intracellular pH (pH). NHE1 uses the energy of allowing an extracellular sodium down its gradient into cells to remove one intracellular proton. The ubiquitous protein has several important physiological and pathological influences on mammalian cells as a result of its activity. The three-dimensional structure of human NHE1 (hNHE1) is not known. Here, we modeled NHE1 based on the structure of MjNhaP1 of Methanocaldoccocus jannaschii in combination with biochemical surface accessibility data. hNHE1 contained 12 transmembrane segments including a characteristic Na/H antiporter fold of two transmembrane segments with a helix - extended region - helix conformation crossing each other within the membrane. Amino acids 363-410 mapped principally to the extracellular surface as an extracellular loop (EL5). A large preponderance of amino acids shown to be surface accessible by biochemical experiments mapped near to, or on, the extracellular surface. Docking of Na/H exchanger inhibitors to the extracellular surface suggested that inhibitor binding on an extracellular site is made up from several amino acids of different regions of the protein. The results present a novel testable, three-dimensional model illustrating NHE1 structure and accounting for experimental biochemical data.

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Structural and Functional Analysis of Transmembrane Segment IV of the Salt Tolerance Protein Sod2*

Cited by 10 publications

References 65 publications

Monovalent cation transporters at the plasma membrane in yeasts

Monovalent cation transporters at the plasma membrane in yeasts

Structure and function of yeast and fungal Na⁺/H⁺ antiporters

Molecular modeling and inhibitor docking analysis of the Na⁺/H⁺exchanger isoform one

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Structural and Functional Analysis of Transmembrane Segment IV of the Salt Tolerance Protein Sod2*

Cited by 10 publications

References 65 publications

Monovalent cation transporters at the plasma membrane in yeasts

Monovalent cation transporters at the plasma membrane in yeasts

Structure and function of yeast and fungal Na+/H+ antiporters

Molecular modeling and inhibitor docking analysis of the Na+/H+exchanger isoform one

Contact Info

Product

Resources

About

Structure and function of yeast and fungal Na⁺/H⁺ antiporters

Molecular modeling and inhibitor docking analysis of the Na⁺/H⁺exchanger isoform one